ID   A1RV12_PYRIL            Unreviewed;       821 AA.
AC   A1RV12;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   SubName: Full=Peptidase M1, membrane alanine aminopeptidase {ECO:0000313|EMBL:ABL88794.1};
GN   OrderedLocusNames=Pisl_1642 {ECO:0000313|EMBL:ABL88794.1};
OS   Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3).
OC   Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=384616 {ECO:0000313|EMBL:ABL88794.1, ECO:0000313|Proteomes:UP000002595};
RN   [1] {ECO:0000313|Proteomes:UP000002595}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4184 / JCM 9189 / GEO3 {ECO:0000313|Proteomes:UP000002595};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Meincke L., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Lowe T., Richardson P.;
RT   "Complete sequence of Pyrobaculum islandicum DSM 4184.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M1 family.
CC       {ECO:0000256|ARBA:ARBA00010136}.
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DR   EMBL; CP000504; ABL88794.1; -; Genomic_DNA.
DR   RefSeq; WP_011763369.1; NC_008701.1.
DR   AlphaFoldDB; A1RV12; -.
DR   STRING; 384616.Pisl_1642; -.
DR   GeneID; 4617971; -.
DR   KEGG; pis:Pisl_1642; -.
DR   eggNOG; arCOG02969; Archaea.
DR   HOGENOM; CLU_014298_0_1_2; -.
DR   OrthoDB; 139771at2157; -.
DR   Proteomes; UP000002595; Chromosome.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd09603; M1_APN_like; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR   InterPro; IPR045357; Aminopeptidase_N-like_N.
DR   InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR004155; PBS_lyase_HEAT.
DR   InterPro; IPR001930; Peptidase_M1.
DR   InterPro; IPR014782; Peptidase_M1_dom.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   PANTHER; PTHR11533:SF303; AMINOPEPTIDASE N; 1.
DR   PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR   Pfam; PF13646; HEAT_2; 3.
DR   Pfam; PF01433; Peptidase_M1; 1.
DR   Pfam; PF17900; Peptidase_M1_N; 1.
DR   PRINTS; PR00756; ALADIPTASE.
DR   SMART; SM00567; EZ_HEAT; 6.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000313|EMBL:ABL88794.1};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          30..189
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          224..444
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   COILED          787..817
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   821 AA;  95622 MW;  2839EFC2753EA241 CRC64;
     MKYLIGRDFA FPEYMPRFPP FYEFDILKMY LNITINIEQR AVEGLVKYRV KAKKDSAKVL
     LDAVEIDLLD VSHEFYYDGE KIEIRPQWKA GEVVEVAVKY RARPRAGMYF VTPHGQRRSV
     YVWTQGESEY NRYWVPLPDS PNIKFPWTVA VTVPKPLVAG SNGLLVEIKE GEDSRTYVWE
     MRHPMSPYLL AIAAGDFEIY SEKCGEVLLE YYIPRYIGGE WRYSFYNTCD IMRFFSEYLG
     VPYPYERYAQ VVVPEFIYGG MENTTFTILT DWTIHDKHAH CPYGEFPCPG QEDFSSDPLV
     AHEMAHMWFG DLVTAKDWGH IAINESFATF IEALWTERSK GREEYLYEIY TNFKTYLGEY
     SRRYSRPIVT NVYKIPDEVF DRHAYEKGSV VLHMLRSLLG DDVFRRGLKV FLERNRYRAV
     DIEDLRKALE EAAGRDLEWF WRQFFYSAGH PVLKISWNYS DGVIKLQIKQ TQGEDSYPVY
     TLPLEIKIVY EDGKRETREI MLDEKEATLH ISGGKPRYIC IDPAFKVMKA LDLQYPLESA
     IAMLDDEDFY CRIQAVEVLK KNGSVKAVDA LARALQDKFW GVATEAAKAL GEIGTAYAVT
     KLIESYHIVS HPRVRRAIVE ALGSSRRKEA AEFLDKILHN QNESYYVRAE AARALGKIKW
     EFAEHSLKRA LEYTSHLDVI KRGALEGLAE LGTDDALKIV LRHTELDMPT YVRVTAVQSL
     AKFGPRREVL ETIRAALRDE NFRVRYAAVT AALELLDQRL IPDLQERMER DVDGRIRRVA
     REVIEKIKRA MERGAEYQKL REEVEKLRDE YRKLLDRIGK H
//